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UniProtKB/Swiss-Prot entry Q8PR33

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LLDD_XANAC
Primary accession number Q8PR33
Secondary accession numbers None
Integrated into Swiss-Prot on January 10, 2006
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 36)
Name and origin of the protein
Protein name L-lactate dehydrogenase [cytochrome]
Synonym EC 1.1.2.3
Gene name
Name: lldD
OrderedLocusNames: XAC0133
From
Xanthomonas axonopodis pv. citri (Citrus canker) [TaxID: 92829] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=306;
DOI=10.1038/417459a; PubMed=12024217 [NCBI, ExPASy, EBI, Israel, Japan]
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.";
Nature 417:459-463(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE011636; AAM35025.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_640489.1; -.
3D structure databases
HSSP P05414; 1GOX. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q8PR33.
Enzyme and pathway databases
BioCyc XAXO190486:XAC0133-MON; -.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0010181; Molecular function: FMN binding (inferred from electronic annotation from InterPro).
GO:0004460; Molecular function: L-lactate dehydrogenase (cytochrome) activity (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01559; -; 1.
PBIL [Tree]
InterPro IPR013785; Aldolase_TIM.
IPR012133; Alpha_OHA_DHase_FMN.
IPR008259; FMN_hydac_DHase_AS.
IPR000262; FMN_OHA_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.70; Aldolase_TIM; 1.
Pfam PF01070; FMN_dh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000138; Al-hdrx_acd_dh; 1.
ProDom PD001005; Triophos_ismrse; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00557; FMN_HYDROXY_ACID_DH_1; 1.
PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 1154204; -.
GenomeReviews AE008923_GR; XAC0133.
KEGG xac:XAC0133; -.
NMPDR fig|190486.1.peg.133; -.
Phylogenomic databases
HOGENOM Q8PR33; -.
Genome annotation databases
CMR Q8PR33; XAC0133.
Other
ProtoNet Q8PR33.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Flavoprotein; FMN; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   388  388     L-lactate dehydrogenase [cytochrome]. PRO_0000206354
DOMAIN   1   380  380     FMN hydroxy acid dehydrogenase. 
NP_BIND   306   330  25     FMN (By similarity). 
ACT_SITE   275   275        Proton acceptor (By similarity). 
BINDING   24    24        Substrate (Potential). 
BINDING   106   106        FMN (By similarity). 
BINDING   127   127        FMN (By similarity). 
BINDING   129   129        Substrate (By similarity). 
BINDING   155   155        FMN (By similarity). 
BINDING   164   164        Substrate (By similarity). 
BINDING   251   251        FMN (By similarity). 
BINDING   278   278        Substrate (Potential). 
Sequence information
Length: 388 AA [This is the length of the unprocessed precursor] Molecular weight: 41830 Da [This is the MW of the unprocessed precursor] CRC64: E60891DE3F3D5FC3 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIISAASDYR AAAEARLPPF LFHYIDGGAY AEHTLRRNVS DLADVALRQR VLRNMSDLRL 

        70         80         90        100        110        120 
STELFGETLA MPVALAPVGL TGMYARRGEV QAARAAAARG IPFTLSTVSV CPIEEVAPAI 

       130        140        150        160        170        180 
ERPMWFQLYV LKDRGFMRNA LERAKAAGVT TLVFTVDMPT PGARYRDAHS GMSGPNASLR 

       190        200        210        220        230        240 
RMLQAVTHPR WAWDVGLLGK PHDLGNISAY RGSPTGLQDY IGWLGANFDP SIAWKDLEWI 

       250        260        270        280        290        300 
REFWTGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGE 

       310        320        330        340        350        360 
LKILADSGIR SGLDVVRMLA LGADAVLLGR AFVYALAAAG QAGVENLLTL IEKEMRVAMT 

       370        380 
LTGTHSIADI SADALSRVTR ERADAISP
Q8PR33 in FASTA format

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